Structure of PDB 1kta Chain B Binding Site BS01

Receptor Information
>1kta Chain B (length=365) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEWNDKGWGQ
PRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRPWLNMDRM
LRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNE
PSLGVSQPRRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGN
YKLGGNYGPTVLVQQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHE
DGVLELVTPPLNGVILPGVVRQSLLDMAQTWGEFRVVERTITMKQLLRAL
EEGRVREVFGSGTACQVCPVHRILYKDRNLHIPTMENGPELILRFQKELK
EIQYGIRAHEWMFPV
Ligand information
Ligand IDKIV
InChIInChI=1S/C5H8O3/c1-3(2)4(6)5(7)8/h3H,1-2H3,(H,7,8)
InChIKeyQHKABHOOEWYVLI-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(C(=O)O)C(C)C
CACTVS 3.341CC(C)C(=O)C(O)=O
OpenEye OEToolkits 1.5.0CC(C)C(=O)C(=O)O
FormulaC5 H8 O3
Name3-METHYL-2-OXOBUTANOIC ACID;
ALPHA-KETOISOVALERIC ACID;
KETOVALINE
ChEMBLCHEMBL146554
DrugBankDB04074
ZINCZINC000001532553
PDB chain1kta Chain B Residue 3001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1kta Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms
Resolution1.9 Å
Binding residue
(original residue number in PDB)		Y570 V655
Binding residue
(residue number reindexed from 1)		Y70 V155
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K702
Catalytic site (residue number reindexed from 1) K202
Enzyme Commision number 2.6.1.42: branched-chain-amino-acid transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004084 branched-chain-amino-acid transaminase activity
GO:0005515 protein binding
GO:0008483 transaminase activity
GO:0052654 L-leucine-2-oxoglutarate transaminase activity
GO:0052655 L-valine-2-oxoglutarate transaminase activity
GO:0052656 L-isoleucine-2-oxoglutarate transaminase activity
Biological Process
GO:0006549 isoleucine metabolic process
GO:0006550 isoleucine catabolic process
GO:0006551 L-leucine metabolic process
GO:0006573 valine metabolic process
GO:0006629 lipid metabolic process
GO:0008652 amino acid biosynthetic process
GO:0009081 branched-chain amino acid metabolic process
GO:0009082 branched-chain amino acid biosynthetic process
GO:0009083 branched-chain amino acid catabolic process
GO:0009098 L-leucine biosynthetic process
GO:0009099 L-valine biosynthetic process
GO:0010817 regulation of hormone levels
GO:1990830 cellular response to leukemia inhibitory factor
Cellular Component
GO:0005654 nucleoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1kta, PDBe:1kta, PDBj:1kta
PDBsum1kta
PubMed12269802
UniProtO15382|BCAT2_HUMAN Branched-chain-amino-acid aminotransferase, mitochondrial (Gene Name=BCAT2)

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